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Helicobacter pylori strain ATCC700392 encodes a methyl-accepting chemotaxis receptor protein (MCP) for arginine and sodium bicarbonate.

作者信息

Cerda Oscar, Rivas Ana, Toledo Héctor

机构信息

Programa de Biología Celular y Molecular, ICBM, Facultad de Medicina, Universidad de Chile, Casilla 70086, Santiago-7, Chile.

出版信息

FEMS Microbiol Lett. 2003 Jul 29;224(2):175-81. doi: 10.1016/S0378-1097(03)00423-3.

Abstract

Helicobacter pylori ATCC43504 responds chemotactically to aspartic acid and serine, but not to arginine, nor to sodium bicarbonate. In contrast, H. pylori ATCC700392 (strain 26695) shows chemotaxis to all four attractants. Open reading frame HP0099 from H. pylori 26695 is predicted to encode one of three methyl-accepting chemotaxis receptor proteins (MCPs). When Escherichia coli is transformed with a plasmid carrying HP0099 from strain 26695, the recombinants acquire chemotaxis to arginine, bicarbonate, and urea. In H. pylori 43504, the HP0099 gene is interrupted with a mini-IS605 insertion, which accounts for its inability to recognize arginine and bicarbonate as attractants. Together, these results argue that the H. pylori HP0099 gene encodes an MCP for arginine and bicarbonate.

摘要

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